Structural highlights
Publication Abstract from PubMed
Helix bundles are among the most widely studied tertiary and quaternary structural motifs in proteins. Here we present the crystal structure of an alpha/beta-peptide foldamer that adopts a tetrameric helix-bundle quaternary structure with a hydrophobic core composed solely of beta-amino acids. The structure displays features that are unprecedented among all known helix bundles composed of either alpha-peptides or peptidic foldamers. The tetramer is characterized by an asymmetry of interaction between neighboring helices, and the side-chain packing within the hydrophobic core differs fundamentally from the knobs-into-holes arrangement typical of most helix bundles.
An alpha/beta-Peptide Helix Bundle with a Pure beta(3)-Amino Acid Core and a Distinctive Quaternary Structure.,Giuliano MW, Horne WS, Gellman SH J Am Chem Soc. 2009 Jul 6. PMID:19580264[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Giuliano MW, Horne WS, Gellman SH. An alpha/beta-Peptide Helix Bundle with a Pure beta(3)-Amino Acid Core and a Distinctive Quaternary Structure. J Am Chem Soc. 2009 Jul 6. PMID:19580264 doi:10.1021/ja8099294
